HSP40-4 Polyclonal Antibody

DNAJA1

DnaJ-like proteins interact with HSP 70 molecular chaperones and function to facilitate protein folding and mitochondrial protein import. HSP 40-4, also known as HDJ2, is the human DnaJ homolog that functions as a co-chaperone with a cysteine-rich zinc finger domain. The cellular redox enzyme thioredoxin interacts with HSP 40-4, and oxidation and reduction reversibly regulate HSP 40-4 function in response to the changing redox states of the cell. The zinc finger domain of HSP 40-4 may act as a redox sensor of chaperone-mediated protein-folding machinery, since HSP 40-4 inactivation leads to the oxidation of cysteine thiols and a simultaneous release of coordinated zinc. Loss of the HSP 40-4 protein may be linked to severe defects in spermatogenesis that involve aberrant androgen signaling.

PBS with 0.05% sodium azide and 50% glycerol, PH7.4

45kDa

0.2 mg/mL

Unconjugated

WB 1:500-1:2000, IHC 1:50-1:200

Recombinant protein of human DNAJA1

Affinity purification

DJ 2;DJ2;DjA1;DnaJ (Hsp40) homolog;subfamily A;member 1;DnaJ homolog subfamily A member 1;DnaJ protein homolog 2;DNAJ2;Dnaja1;DNJA1;hDJ 2;HDJ-2;HDJ2;Heat shock 40 kDa protein 4;heat shock protein DNAJ like 2;Heat shock protein J2;HSDJ;HSJ-2;HSJ2;HSPF4;Human DnaJ protein 2;NEDD7;Neural precursor cell expressed developmentally down regulated 7;OTTHUMP00000021193

P31689